Structure of myotoxin II, a catalytically inactive Lys49 phospholipase A2 homologue from Atropoides nummifer venom
Carregando...
Data
Orientador
Coorientador
Pós-graduação
Curso de graduação
Título da Revista
ISSN da Revista
Título de Volume
Editor
International Union of Crystallography (IUCr)
Tipo
Artigo
Direito de acesso
Acesso aberto
Resumo
Lys49 snake-venom phospholipase A2 (PLA2) homologues are highly myotoxic proteins which, although lacking catalytic activity, possess the ability to disrupt biological membranes, inducing significant muscle-tissue loss and permanent disability in severely envenomed patients. Since the structural basis for their toxic activity is still only partially understood, the structure of myotoxin II, a monomeric Lys49 PLA2 homologue from Atropoides nummifer, has been determined at 2.08 Å resolution and the anion-binding site has been characterized. © 2006 International Union of Crystallography. All rights reserved.
Descrição
Palavras-chave
Atropoides nummifer myotoxin II, Atropoides nummifer phospholipase A snake venom amino acid sequence binding site chemistry crystallization molecular genetics sequence alignment X ray crystallography Amino Acid Sequence Binding Sites Crotalid Venoms Crystallization Crystallography, X-Ray Molecular Sequence Data Phospholipases A Sequence Alignment
Idioma
Inglês
Citação
Acta Crystallographica Section F: Structural Biology and Crystallization Communications, v. 62, n. 5, p. 423-426, 2006.
